Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.1.27.1 (RNase)
16,360 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Serum amylase continues to be the most widely used test to diagnose acute pancreatitis; however, its popularity does not appear to be justified. The serum amylase test has a poor sensitivity and specificity. Furthermore, it has an extremely low sensitivity in detecting acute alcoholic pancreatitis, which is the most common cause of acute pancreatitis in city hospitals. Older assay techniques for serum lipase were cumbersome and time-consuming. The newer methods seem to have overcome the disadvantages of the previous techniques. They are quick, reliable, and inexpensive. Recent studies indicate that serum lipase may be a better test to diagnose acute pancreatitis. Therefore, serum lipase should be used more frequently in the diagnosis of acute pancreatitis. Serum trypsin, although sensitive, is difficult to estimate and is not routinely available. Serum elastase offers no additional benefit over the serum amylase or lipase tests. Markers such as alpha 2-macroglobulin, RNase, phospholipase, and polymorphonuclear elastase predict severity of disease, but assay techniques for these agents are still experimental and confined to specialized centers. C-reactive protein is a reasonably reliable indicator of severity and, because it is universally available, should be used more frequently. Of the imaging techniques, computerized tomography scanning is the best method to delineate the pancreas; however, ultrasound is more cost-effective in clinical practice.
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PMID:Diagnostic tests for acute pancreatitis. 805 37

In the previous studies we have shown that testosterone increases lipolytic responsiveness to catecholamines in rat white adipocytes, and that is associated with an up-regulation of beta-adrenergic receptor density. However, the postreceptor events involved in the testosterone induced enhancement of beta-adrenergic receptor activated lipolysis in these cells have not been adequately studied, and were therefore investigated in the present study. Male Sprague Dawley rats were divided into three groups: control, castrated, and castrated treated with testosterone. The beta-adrenergic receptor-mediated cAMP accumulation, measured with RIA after isoproterenol (a beta-adrenergic agonist) stimulation was decreased in castrated rats, and reversed by testosterone treatment, suggesting a testosterone effect at or proximal to adenylate cyclase. However, no differences between the groups were found in abundance of G alpha protein messenger RNAs (G alpha s, G alpha i-1, and G alpha i-2) as analyzed by Northern blot and a solution hybridization RNase protection assay, or in G protein mass measured with a quantitative enzyme-linked immunosorbent assay in fat cell membrane preparation. Lipolysis stimulated by N6-monobutyryl-cAMP was reduced in castrated rats and recovered by testosterone treatment, suggesting that components distal to the adenylate cyclase, i.e. protein kinase A (PKA) and/or hormone sensitive lipase (HSL) also are involved in testosterone regulation of lipolysis. In conclusion, these and previous results suggest that the testosterone-induced increase in lipolytic response to catecholamines in rat white adipocytes is mediated through several events including an increased beta-adrenergic receptor density, probably an increased adenylate cyclase activity and an increased protein kinase A/hormone sensitive lipase activity at the postreceptor level with apparent absence of effect on the expression of G-proteins.
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PMID:Postreceptor events involved in the up-regulation of beta-adrenergic receptor mediated lipolysis by testosterone in rat white adipocytes. 838 92

Beining, Paul R. (The Catholic University of America, Washington, D.C.) and E. R. Kennedy. Characteristics of a strain of Staphylococcus aureus grown in vivo and in vitro. J. Bacteriol. 85:732-741. 1963.-A comparative survey was conducted on the characteristics of a strain of Staphylococcus aureus after it had been grown in vitro (VSB) and after it had been collected from the peritoneal exudate of an infected guinea pig (GSB). Both VSB and GSB strains gave the same results when studied in an extensive series of tests, including bound and soluble coagulases, bacteriophage type, antibiotic-sensitivity pattern, the usual fermentation reactions, deoxyribonucleic acid base composition, and qualitative tests for hemolysins, deoxyribonuclease, ribonuclease, staphylokinase, staphyloprotease, lipase, and phosphatase. The in vivo strain differed significantly from the in vitro strain in respiratory rate, agar gel diffusion studies, agglutinability in tube tests, virulence tests in rabbits and mice, growth on tellurite-glycine agar, susceptibility to human gamma-globulin in agar, and in the quantitative production of deoxyribonuclease, alpha-hemolysin, leucocidin, and hyaluronidase.
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PMID:CHARACTERISTICS OF A STRAIN OF STAPHYLOCOCCUS AUREUS GROWN IN VIVO AND IN VITRO. 1404 37

The contents of selected hydrolytic enzymes of oil-induced peritoneal, normal alveolar, and BCG-induced alveolar macrophages have been studied. On a per cell or nitrogen basis the normal alveolar cells contained considerably more acid phosphatase, cathepsin, acid ribonuclease, lysozyme, and lipase than peritoneal cells. The BCG-induced alveolar macrophage exhibited increased levels of acid phosphatase, lysozyme, and lipase as compared to alveolar macrophages from unstimulated rabbits. The morphological differences between these cells was discussed and electron micrographs of the BCG-induced macrophage presented. Fractionation of the BCG-induced macrophage by differential centrifugation showed that 60 to 80 per cent of the total cell content of acid phosphatase, cathepsin, beta glucuronidase, acid ribonuclease, acid deoxyribonuclease, aryl sulfatase, lysozyme, and lipase were localized in a postnuclear fraction which sedimented at 15,000 g. This fraction also contained the majority of the mitochondria as evidenced by its content of cytochrome oxidase. Non-specific esterase was not localized to this fraction. A separation of the hydrolase-containing particles and mitochondria was achieved by isopycnic sucrose gradient centrifugation. Under the conditions employed, the mitochondria distributed at densities of 1.19 to 1.20, whereas the hydrolase particles sedimented to a density of 1.26 to 1.27. Each of the hydrolases including acid phosphatase, beta glucuronidase, cathepsin, lysozyme, and acid ribonuclease exhibited maximum activities in the same gradient fraction. The isolated granules exhibited enzymatic latency, and activation could be achieved by cycles of freezing and thawing or surface active agents. The majority of each of the hydrolytic enzymes could be liberated in a non-particulate form by mechanical trauma. Macrophages which had been stained supravitally with neutral red were fractionated by differential and gradient centrifugation. More than 70 per cent of the dye could be recovered in the particulate hydrolase fraction. The isolated, stained granules resembled those seen in the intact cell.
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PMID:THE PARTICULATE HYDROLASES OF MACROPHAGES. I. COMPARATIVE ENZYMOLOGY, ISOLATION, AND PROPERTIES. 1411 77

Legionella pneumophila, the gram-negative agent of Legionnaires' disease, possesses type IV pili and a type II protein secretion (Lsp) system, both of which are dependent upon the PilD prepilin peptidase. By analyzing multiple pilD mutants and various types of Lsp mutants as well as performing trans-complementation of these mutants, we have confirmed that PilD and type II secretion genes are required for L. pneumophila infection of both amoebae and human macrophages. Based upon a complete analysis of lspDE, lspF, and lspG mutants, we found that the type II system controls the secretion of protease, RNase, lipase, phospholipase A, phospholipase C, lysophospholipase A, and tartrate-sensitive and tartrate-resistant acid phosphatase activities and influences the appearance of colonies. Examination of the developing L. pneumophila genome database indicated that the organism has two other loci (lspC and lspLM) that are predicted to promote secretion and thus a set of genes that is comparable to the type II secretion genes in other gram-negative bacteria. In contrast to lsp mutants, L. pneumophila pilus mutants lacking either the PilQ secretin, the PspA pseudopilin, or pilin were not defective for colonial growth, secreted activities, or intracellular replication. L. pneumophila dot/icm mutants were also not impaired for type II-dependent exoenzymes. Upon intratracheal inoculation into A/J mice, lspDE, lspF, and pilD mutants, but not pilus mutants, exhibited a reduced ability to grow in the lung, as measured by competition assays. The lspF mutant was also defective in an in vivo kinetic assay. Examination of infected mouse sera revealed that type II secreted proteins are expressed in vivo. Thus, the L. pneumophila Lsp system is a virulence factor and the only type II secretion system linked to intracellular infection.
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PMID:Legionella pneumophila type II protein secretion promotes virulence in the A/J mouse model of Legionnaires' disease pneumonia. 1468 10

Grapefruit seed extract (GSE) has been shown to exert antibacterial, antifungal and antioxidant activity possibly due to the presence of naringenin, the flavonoid with cytoprotective action on the gastric mucosa. No study so far has been undertaken to determine whether this GSE is also capable of preventing acute pancreatic damage induced by ischemia/reperfusion (I/R), which is known to result from reduction of anti-oxidative capability of pancreatic tissue, and whether its possible preventive effect involves an antioxidative action of this biocomponent. In this study carried out on rats with acute hemorrhagic pancreatitis induced by 30 min partial pancreatic ischemia followed by 6 h of reperfusion, the GSE or vehicle (vegetable glycerin) was applied intragastrically in gradually increasing amounts (50-500 microl) 30 min before I/R. Pretreatment with GSE decreased the extent of pancreatitis with maximal protective effect of GSE at the dose 250 microl. GSE reduced the pancreatitis-evoked increase in serum lipase and poly-C specific ribonuclease activity, and attenuated the marked fall in pancreatic blood flow and pancreatic DNA synthesis. GSE administered alone increased significantly pancreatic tissue content of lipid peroxidation products, malondialdehyde and 4-hydroxyalkens, and when administered before I/R, GSE reduced the pancreatitis-induced lipid peroxidation. We conclude that GSE exerts protective activity against I/R-induced pancreatitis probably due to the activation of antioxidative mechanisms in the pancreas and the improvement of pancreatic blood flow.
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PMID:Extract of grapefruit-seed reduces acute pancreatitis induced by ischemia/reperfusion in rats: possible implication of tissue antioxidants. 1561 45

Based on inorganic matrix controlled pore glass (CPG) and macro-pore silica sphere, by using polyethylene glycol (PEG 1000) as a ligand, a preparation method of hydrophobic interaction chromatographic (HIC) packing material was improved by adding a proper catalyst during the bonding process. The packing material can be synthesized in a scale-up batch, for example 150g for each batch, both for analytical and preparative columns. The retention of proteins, such as cytochrome C (Cyt-C), chymotrypsingen-A (Chy-A), lysozyme (Lys) and ribonuclease(Rnase), is increased with the increasing of (NH4)2SO4 concentration in the eluant 2.5 mol/L of salt concentration for the mobile phase was chosen by considering the separation efficiency and equipment life. After comparing the effect of pH for the retention of proteins it is found that the proteins are well separated at pH 7. The time of linear gradient elution program was optimized in considering the separation efficiency and speed. It is better to take 30 minutes of the gradient program for the separation. Six standard proteins can be well separated with the high-performance HIC column in the linear gradient elution program from 2.5 to 0 mol/L of (NH4)2SO4 in 50 mmol/L of phosphate buffer solution within 30 minutes. Cyt-C, Rnase, Lys and Chy-A can be separated by the HIC column based on CPG matrix. Six proteins, Cyt-C, Rnase, Lys, Chy-A, insulin(Ins) and lipase (Lip) can be well separated on the column based on silica matrix with gradient elution program. The recovery of trypsin detected with BAEE method is over 95% after purification with the HIC column.
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PMID:[Scale-up preparation of hydrophobic interaction chromatographic packing materials based on inorganic matrix]. 1573 63

Legionella pneumophila possesses a variety of secreted and cell-associated hydrolytic activities that could be involved in pathogenesis. The activities include phospholipase A, lysophospholipase A, glycerophospholipid:cholesterol acyltransferase, lipase, protease, phosphatase, RNase, and p-nitrophenylphosphorylcholine (p-NPPC) hydrolase. Up to now, there have been no data available on the regulation of the enzymes in L. pneumophila and no data at all concerning the regulation of bacterial phospholipases A. Therefore, we used L. pneumophila mutants in the genes coding for the global regulatory proteins RpoS and LetA to investigate the dependency of hydrolytic activities on a global regulatory network proposed to control important virulence traits in L. pneumophila. Our results show that both L. pneumophila rpoS and letA mutants exhibit on the one hand a dramatic reduction of secreted phospholipase A and glycerophospholipid:cholesterol acyltransferase activities, while on the other hand secreted lysophospholipase A and lipase activities were significantly increased during late logarithmic growth phase. The cell-associated phospholipase A, lysophospholipase A, and p-NPPC hydrolase activities, as well as the secreted protease, phosphatase, and p-NPPC hydrolase activities were significantly decreased in both of the mutant strains. Only cell-associated phosphatase activity was slightly increased. In contrast, RNase activity was not affected. The expression of plaC, coding for a secreted acyltransferase, phospholipase A, and lysophospholipase A, was found to be regulated by LetA and RpoS. In conclusion, our results show that RpoS and LetA affect phospholipase A, lysophospholipase A, acyltransferase, and other hydrolytic activities of L. pneumophila in a similar way, thereby corroborating the existence of the LetA/RpoS regulation cascade.
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PMID:The global regulatory proteins LetA and RpoS control phospholipase A, lysophospholipase A, acyltransferase, and other hydrolytic activities of Legionella pneumophila JR32. 1645 2

The mouse-protective activity of Erysipelothrix rhusiopathiae culture supernatant fluids exists in a polydisperse form, ranging in density from aggregates which sediment at 10,000 x g for 3 hr to soluble units which will not sediment at 198,000 x g for 12 hr. A partially purified protective antigen has been isolated from the aggregates sedimented from a concentrate of the culture supernatant fluid at 20,000 x g for 3 hr. These aggregates contained the major protective antigen or antigens of E. rhusiopathiae, since, in addition to inducing active immunity, they adsorbed essentially all of the passively protecting antibody from rabbit antiserum produced by immunization with whole culture. The protective activity in these aggregates was destroyed by trypsin and greatly diminished by muramidase and heating at 64 C, but was not affected by lipase or ribonuclease.
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PMID:Isolation and Characterization of a Protective Antigen-Containing Particle from Culture Supernatant Fluids of Erysipelothrix rhusiopathiae. 1655 45

Protector-II (Pr-II) of the Japanese morning glory (Pharbitis nil Choisy) was inactivated by exposure to polyphenol oxidase. An unidentified protector in the same molecular weight range obtained from sunflower was also inactivated by this enzyme. Earlier speculations that protectors might be lipoprotein in nature were negated by the fact that neither lipase nor protease inactivated the protectors. The protectors were also not inactivated by incubating with alpha-amylase, DNase, or RNase. Catechol mimics Pr and is inactivated by polyphenol oxidase. The oxidation of catechol to o-quinone is accompanied by a loss of chromophores that absorb ultraviolet light and the appearance of a reddish brown color. Similarly, when the relatively low molecular weight auxin protectors (Pr-II class) were incubated with polyphenol oxidase, their oxidation was also frequently associated with the formation of brown color, and oxidation with H(2)O(2) caused a loss of ultraviolet-absorbing chromophores. The data indicate that auxin protectors contain o-dihydroxyphenolic groups at their active site.That o-dihydroxyphenols inhibit indoleacetic acid oxidation has been demonstrated by numerous workers. It is suggested that the high molecular weight auxin protectors and the phenolic compounds described by other authors comprise part of a metabolic system concerned with the regulation of peroxidase-catalyzed redox reactions.
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PMID:Studies on Auxin Protectors: IX. Inactivation of Certain Protectors by Polyphenol Oxidase. 1665 85


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